Effect of pH-shifting treatment on structural and heat induced gel properties of peanut protein isolate

Li, Junguang; Wu, Mengmeng; Wang, Yuntao; Li, Ke; Du, Juan; Bai, Yanhong

doi:10.1016/j.foodchem.2020.126921

Cited by 159 publications

(91 citation statements)

References 53 publications

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“…As shown in the paper, the solubility of hemp seed protein isolate increased from 20.6 % to 97.5 % after a combined pH 12 shift and heating treatment at 80 °C for 60 min [12]. The study showed that pH-shifting treatment can improve the solubility of peanut protein from 79.39 % to 89.87 % [13]. All these investigations showed that pH-shifting treatment is a good way to improve the solubility of plant proteins.…”

Section: Literature Review and Problem Statementmentioning

confidence: 58%

“…This might be due to that some polar groups (such as carboxyl and amide groups) were buried after pH-shifting treatment at pH 2, pH 4, pH 10, and pH 12, as a result, the interaction ability with water was decreased [16]. It has been reported that the solubility of peanut protein isolate also showed decreased (p<0.05) value after pH-shifting treatment at pH 2 and pH 12 [13].…”

Section: Results Of Determining the Solubility Of Pumpkin Seed Protein Isolatementioning

confidence: 97%

“…The particle size distribution and zeta potential of soluble protein in PSPI were determined by the Zetasizer Nano-ZS90 (Malvern Instrument Ltd., UK) following the previously described method with minor modification [13]. The PSPI (1.0 mg/mL, w/v, pH 7.0) dispersion was stirred for 1 h at 25 °C and then centrifuged (10000×g) for 15 min to get the supernatant.…”

Section: Methodsmentioning

confidence: 99%

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Determining the effect of pH-shifting treatment on the solubility of pumpkin seed protein isolate

Гао

Helikh

Duan

2021

EEJET

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Pumpkin seed protein is a high-quality plant protein, which has all essential amino acids for the human body and can also supply essential amino acid histidine for children. When it is introduced to food products, it needs to meet some functional properties, such as solubility, emulsifying ability, foaming ability, and so on. Among them, solubility is very important because it has a great influence on other functional properties of protein. In this study, pH-shifting treatment, which is a novel method to modify protein, is applied to improve the solubility of pumpkin seed protein isolate (PSPI). PSPI treated by pH-shifting treatment was investigated at different pH values (pH 2, pH 4, pH 6, pH 8, pH 10, and pH 12), which were labeled as PSPI 2, PSPI 4, PSPI 6, PSPI 8, PSPI 10, and PSPI 12, respectively. Compared to that of control PSPI (45.6 %), only the solubility of PSPI 8 (55.5 %) showed increased (p<0.05) value, while the solubility of PSPI 2 (13.7 %), PSPI 4 (10.8 %), PSPI 10 (41.8 %), and PSPI 12 (13.4 %) showed decreased (p<0.05) value. Then the average particle size, zeta potential of the soluble protein in PSPI were analyzed, and sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) was performed. PSPI 2, PSPI 4, and PSPI 12 showed decreased (p<0.05) average particle size after the pH-shifting process. And PSPI 2, and PSPI 12 showed decreased (p<0.05) zeta potential. While other samples didn’t show any significant difference in these two indicators. Besides, the molecular weight of the increased abundance of soluble protein bands was observed at 33 kDa and 25 kDa of PSPI 8. As the solubility of PSPI 8 increased (p<0.05) significantly, it might suggest the PSPI after pH-shifting treatment under pH 8 has more advantages to be used in the food industry

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Section: Literature Review and Problem Statementmentioning

confidence: 58%

Section: Results Of Determining the Solubility Of Pumpkin Seed Protein Isolatementioning

confidence: 97%

Section: Methodsmentioning

confidence: 99%

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Determining the effect of pH-shifting treatment on the solubility of pumpkin seed protein isolate

Гао

Helikh

Duan

2021

EEJET

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“…The introduction of the pH-shifting method is of great significance to improve the gel properties of peanut protein isolate. It was found that the breaking force and water-holding capacity of the pea protein gel improved significantly due to the reduced particle size, enhanced solubility, free sulfhydryl group concentration, and surface hydrophobicity when the peanut protein isolate was subjected to pH shifting [144]. In another study, pH shifting seemed to enhance the protein solubility in soy; however, the effect of pH shifting was low when the ionic strength was high and the pH was between 4 and 7 [145].…”

Section: Glycationmentioning

confidence: 99%

Plant Proteins for Future Foods: A Roadmap

Sim

Srv

Chiang

et al. 2021

Foods

149

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Protein calories consumed by people all over the world approximate 15–20% of their energy intake. This makes protein a major nutritional imperative. Today, we are facing an unprecedented challenge to produce and distribute adequate protein to feed over nine billion people by 2050, in an environmentally sustainable and affordable way. Plant-based proteins present a promising solution to our nutritional needs due to their long history of crop use and cultivation, lower cost of production, and easy access in many parts of the world. However, plant proteins have comparatively poor functionality, defined as poor solubility, foaming, emulsifying, and gelling properties, limiting their use in food products. Relative to animal proteins, including dairy products, plant protein technology is still in its infancy. To bridge this gap, advances in plant protein ingredient development and the knowledge to construct plant-based foods are sorely needed. This review focuses on some salient features in the science and technology of plant proteins, providing the current state of the art and highlighting new research directions. It focuses on how manipulating plant protein structures during protein extraction, fractionation, and modification can considerably enhance protein functionality. To create novel plant-based foods, important considerations such as protein–polysaccharide interactions, the inclusion of plant protein-generated flavors, and some novel techniques to structure plant proteins are discussed. Finally, the attention to nutrition as a compass to navigate the plant protein roadmap is also considered.

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“…Li et al . (2020) studied pH‐shift treatment on heat‐induced gel properties of peanut protein isolates. It was indicated that peanut protein isolates treated at pH 10 improved breaking force and water‐holding capacity of formed gel.…”

Section: Functional Characteristics Of Proteins Modified By Ph‐shift mentioning

confidence: 99%

Physicochemical and functional characteristics of proteins treated by a pH‐shift process: a review

Tang

Ying

Shi

2020

Int J of Food Sci Tech

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Summary Advanced structures of food proteins are maintained by many forces such as hydrophobic activities, electrostatic interaction, and disulphide bond interaction, which can affect their functional characteristics to a certain extent. Therefore, many approaches have been utilised to improve functional characteristics of food proteins. pH‐shift process refers to the method that food proteins are treated under extreme alkaline or acid conditions followed by adjusting pH to isoelectric point or neutral pH. Many studies have showed that pH‐shift process can significantly affect the functional characteristics of food proteins, for example emulsifying activities, forming property, solubility and water/oil adsorption ability. pH‐shift process has been utilised to recover protein isolates from many sources including fish, fish by‐products, meat processing products. Many researches have indicated that the functional and physicochemical characteristics of recovered protein isolates are significantly influenced by pH‐shift process. In this paper, the latest studies regarding the functional and physicochemical characteristics of proteins treated or recovered through pH‐shift process, and potential applications of obtained protein isolates in the production of the hydrolysates or used as a delivery system were reviewed.

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Effect of pH-shifting treatment on structural and heat induced gel properties of peanut protein isolate

Cited by 159 publications

References 53 publications

Determining the effect of pH-shifting treatment on the solubility of pumpkin seed protein isolate

Determining the effect of pH-shifting treatment on the solubility of pumpkin seed protein isolate

Plant Proteins for Future Foods: A Roadmap

Physicochemical and functional characteristics of proteins treated by a pH‐shift process: a review

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